✦ LIBER ✦

Substrate-Dependent Unfolding of the Energy Coupling Motif of a Membrane Transport Protein Determined by Double Electron-Electron Resonance †

✍ Scribed by Xu, Qi; Ellena, Jeffrey F.; Kim, Miyeon; Cafiso, David S.

Book ID: 126872206
Publisher: American Chemical Society
Year: 2006
Tongue: English
Weight: 355 KB
Volume: 45
Category: Article
ISSN: 0006-2960
DOI: 10.1021/bi061051x

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Interresidual Distance Determination by

Interresidual Distance Determination by Four-Pulse Double Electron-Electron Resonance in an Integral Membrane Protein: The Na+/Proline Transporter PutP of Escherichia coli

✍ Jeschke, Gunnar; Wegener, Christoph; Nietschke, Monika; Jung, Heinrich; Steinhof 📂 Article 📅 2004 🏛 Biophysical Society 🌐 English ⚖ 152 KB

Structure and conformation of the nitrox

Structure and conformation of the nitroxyl spin-label ethyl 3-(2,2,5,5-tetramethylpyrrolinyl-1-oxyl)-propen-2-oate determined by electron nuclear double resonance: Comparison with the structure of a spin-label substrate of carboxypeptidase A

✍ Devkumar Mustafi; William E. Boisvert; Marvin W. Makinen 📂 Article 📅 1990 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 857 KB

The conformation of the nitroxyl spin-label ethyi 3-(2,2,5,5-tetramethylpyrrolinyl-1-oxy1)-propen-2-oate has been determined by electron nuclear double resonance (ENDOR) spectroscopy and computer-based molecular modeling. From ENDOR spectra of the compound in frozen solution, we have assigned resona